ArticleThe Journal of biological chemistry2012
Matrix metalloproteinase-2 cleavage of the β1 integrin ectodomain facilitates colon cancer cell motility.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 75 citations in OpenAlex.
- MMP7-mediated cleavage of nucleolin at Asp255 induces MMP9 expression to promote tumor malignancy.Oncogene · 2015Trial
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- Integrins in cancer: insights into mechanisms and therapeutic potential.Cell communication and signaling : CCS · 2026Review
- Using 3D Invasion properties of RCC Cell Lines In Vitro to predict their Metastatic Potential In Vivo.Cell death discovery · 2026Article
- Integration of cAMP and TRPV4 Signaling to Optimize Collagen Remodeling for Management of Fibrosis.Cells · 2025Review
- The function of metalloproteinases in pathophysiology of inflammatory bowel disease and colon cancer.Journal of leukocyte biology · 2025Review
- Gelatin In Situ Zymography to Study Gelatinase Activity in Colon Cancer Cells Treated with Platelet Microparticles (PMPs).Methods in molecular biology (Clifton, N.J.) · 2024Article
- New thoughts and findings on invasion and metastasis of pancreatic ductal adenocarcinoma (PDAC) from comparative proteomics: multi-target therapy.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2023Review
- Insights into the Role of Matrix Metalloproteinases in Precancerous Conditions and in Colorectal Cancer.Cancers · 2021Review
- A preliminary study of possible fibrotic role of meprin metalloproteases in scleroderma patients.Archives of rheumatology · 2021Article
- Assessment of clinical variables as predictive markers in the development and progression of colorectal cancer.Bioengineered · 2021Article
- Folic Acid-Targeted Paclitaxel-Polymer Conjugates Exert Selective Cytotoxicity and Modulate Invasiveness of Colon Cancer Cells.Pharmaceutics · 2021Article
- Quantitative Proteomics Reveals Changes Induced by TIMP-3 on Cell Membrane Composition and Novel Metalloprotease Substrates.International journal of molecular sciences · 2021Article
- Differential inhibition of gelatinase activity in human colon adenocarcinoma cells by Aloe vera and Aloe arborescens extracts.BMC complementary medicine and therapies · 2020Article
- Matrix Metalloprotease-7 Mediates Nucleolar Assembly and Intra-nucleolar Cleaving p53 in Gefitinib-Resistant Cancer Stem Cells.iScience · 2020Article
- Mandibular undifferentiated pleomorphic sarcoma: Molecular analysis of a primary cell population.Clinical and experimental dental research · 2020Article
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- Scarring vs. functional healing: Matrix-based strategies to regulate tissue repair.Advanced drug delivery reviews · 2018Review
- Epidermal growth factor-mediated Rab25 pathway regulates integrin β1 trafficking in colon cancer.Cancer cell international · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cancer cell invasion is a key element in metastasis that requires integrins for adhesion/de-adhesion, as well as matrix metalloproteinases (MMPs) for focalized proteolysis. Herein we show that MMP-2 is up-regulated in resected colorectal tumors and degrades β1 integrins with the release of fragments containing the β1 I-domain. The β1 cleavage pattern is similar to that produced by digestion of α5β1 and α2β1 with MMP-2. Two such fragments, at 25 and 75 kDa, were identified after immunoprecipitation, with monoclonal antibody BD610468 reacting with the NH(2)-terminal I-like ectodomain followed by SDS-PAGE and microsequencing using electrospray (ISI-Q-TOF-Micromass) spectrometry. Cleavage of the β1 integrin can be abolished by inhibition of MMP-2 activity; it can be induced by up-regulation of MMP-2 expression, as exemplified by HT29 colon cancer cells transfected with pCMV6-XL5-MMP-2. Co-immunoprecipitation studies of colon cancer cells showed that the β1 integrin subunit is associated with MMP-2. The MMP-2-mediated shedding of the I-like domain from β1 integrins resulted in decreased adhesion of colon cancer cells to collagen and fibronectin, thus abolishing their receptivity. Furthermore, such cells showed enhanced motility as evaluated by a "wound healing-like" assay and time-lapse microscopy, indicating their increased invasiveness. Altogether, our data demonstrate that MMP-2 amplifies the motility of colon cancer cells, not only by digesting the extracellular matrix components in the vicinity of cancer cells but also by inactivating their major β1 integrin receptors.
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